Anti-Hu PAG1 Purified

PAG (phosphoprotein associated with GEMs), also known as Cbp (Csk-binding protein), is a ubiquitously expressed 46 kDa transmembrane adaptor protein present in membrane rafts (glycosphingolipid-enriched microdomains), which however migrates on SDS PAGE gels anomalously as an 80 kDa molecule. Following tyrosine phosphorylation by Src family kinases, PAG binds and thereby activates the protein tyrosine kinase Csk, the major negative regulator of the Src family kinases. Signaling via the B-cell receptor in B cells or high affinity IgE receptor (FcepsilonRI) in mast cells leads to PAG increased tyrosine phosphorylation and Csk binding, while T cell receptor signaling causes PAG dephosphorylation, loss of Csk binding and increased activation of the protein tyrosine kinase Lck.

Product Specifications

Certification

RUO

Negative Species

Mouse,Rat,Cow

Reactivity

Human

Immunogen

Recombinant intracellular fragment (aa 97-432) of human Cbp (PAG) .

Target Antigen

PAG1

Clone

MEM-255

Applications

WB, IHC-P, FC-IC

Concentration

1 mg/mL

Format

Purified

Buffer

Phosphate buffered saline (PBS), pH 7.4, 15 mM sodium azide

References & Citations

*Semac I, Palomba C, Kulangara K, Klages N, van Echten-Deckert G, Borisch B, Hoessli DC: Anti-CD20 therapeutic antibody rituximab modifies the functional organization of rafts/microdomains of B lymphoma cells. Cancer Res. 2003 Jan 15;63 (2) :534-40., URL: https://www.ncbi.nlm.nih.gov/pubmed/12543813?dopt=, *Brdicka T, Pavlistova D, Leo A, Bruyns E, Korinek V, Angelisova P, Scherer J, Shevchenko A, Hilgert I, Cerny J, Drbal K, Kuramitsu Y, Kornacker B, Horejsi V, Schraven B: Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation. J Exp Med. 2000 May 1;191 (9) :1591-604., URL: https://www.ncbi.nlm.nih.gov/pubmed/10790433?dopt=, *Brdickova N, Brdicka T, Andera L, Spicka J, Angelisova P, Milgram SL, Horejsi V: Interaction between two adapter proteins, PAG and EBP50: a possible link between membrane rafts and actin cytoskeleton. FEBS Lett. 2001 Oct 26;507 (2) :133-6., URL: https://www.ncbi.nlm.nih.gov/pubmed/11684085?dopt=, *Schatzlmaier P, Supper V, Göschl L, Zwirzitz A, Eckerstorfer P, Ellmeier W, Huppa JB, Stockinger H: Rapid multiplex analysis of lipid raft components with single-cell resolution. Sci Signal. 2015 Sep 22;8 (395) :rs11, URL: http://www.ncbi.nlm.nih.gov/pubmed/26396269 , *Svec A, Velenská Z, Horejsí V: Expression pattern of adaptor protein PAG: correlation between secondary lymphatic follicle and histogenetically related malignant lymphomas. Immunol Lett. 2005 Aug 15;100 (1) :94-7., URL: http://www.ncbi.nlm.nih.gov/pubmed?term=svec%20velenska%20horejsi , *Tedoldi S, Paterson JC, Hansmann ML, Natkunam Y, Rudiger T, Angelisova P, Du MQ, Roberton H, Roncador G, Sanchez L, Pozzobon M, Masir N, Barry R, Pileri S, Mason DY, Marafioti T, Horejsi V: Transmembrane adaptor molecules: a new category of lymphoid-cell markers. Blood. 2006 Jan 1;107 (1) :213-21. Epub 2005 Sep 13., URL: https://www.ncbi.nlm.nih.gov/pubmed/16160011?dopt=, *Davidson D, Bakinowski M, Thomas ML, Horejsi V, Veillette A: Phosphorylation-dependent regulation of T-cell activation by PAG/Cbp, a lipid raft-associated transmembrane adaptor. Mol Cell Biol. 2003 Mar;23 (6) :2017-28., URL: https://www.ncbi.nlm.nih.gov/pubmed/12612075?dopt=

Storage Conditions

Store at 2-8°C. Do not freeze.

Specificity

The antibody MEM-255 recognizes an epitope (aa 235-280) of Csk-binding protein (Cbp) located in the cytoplasmic domain, also known as protein associated with glycosphingolipid-enriched microdomains (PAG) .

Applications Notes

Flow cytometry: Recommended dilution: 2 μg/ml. Intracellular staining.Immunohistochemistry (paraffin sections) : Positive tissue: tonsil, spleen. Western blotting: Csk binding protein is an ubiquitously expressed 46 kDa transmembrane adaptor protein present in membrane microdomains (rafts), which, however, migrates on SDS-PAGE gels anomalously as an 80 kDa molecule.